X-ray diffraction data are being collected best to 2.9 E from crystals of ribosomes, their complexes, mimicking defined functional states (e.g., 70S ribosomes with a short mRNA and two charged tRNA molecules), their native and their mutated, depleted and modified subunits, at cryo-temperature, using intense synchrotron radiation sources. Quantitative multi-metal cluster binding led to an SIR map at low resolution. Data collected from crystals soaked in solutions of multi-metal salts, led to an interpretable difference Patterson map at medium resolution. Parallel low resolution phasing by direct methods, rotation searches and solvent contrast variation, led to the construction of an envelope, showing striking similarity to that observed by electron microscopy.